Joshua's Research

12.09.11

Compound1.jpg
A: no enzyme control, B and C: no compound 1 controls. Conditions common to all reactions: 50 mM Tris-acetate, 10 mM MgCl2, 0.5 mM pNPP, and 76.42 nM (2.5 ng/mL) MptpB (except for condition A). A: 0.1 mM compound 1, B and C: 50% DMSO in lieu of compound 1, D: 0.1 mM compound 1, F: 0.3 mM compound 1, G: 0.4 mM compound 1, H: 0.6 mM compound 1, 0.001 mM Orthovanadate

Reaction condition E absent from graph above because it was spilled.

Compound2.jpg
A: no enzyme control, B and C: no compound 2 controls. Conditions common to all reactions: 50 mM Tris-acetate, 10 mM MgCl2, 0.5 mM pNPP, and 76.42 nM (2.5 ng/mL) MptpB (except for condition A). A: 0.1 mM compound 2, B and C: 50% DMSO in lieu of compound 2, D: 0.1 mM compound 2, E: 0.2 mM compound 2, F: 0.3 mM compound 2, G: 0.4 mM compound 2, H: 0.6 mM compound 2, 0.001 mM Orthovanadate




Week 14:

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MptpB enzyme assay with pNPP as surrogate substrate


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MptpB enzyme assay with pNPP as surrogate substrate




Week 13:

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ICM screening of cb_306 against chain A of 2ZO5 (PDB ID of open conformation of MptpB)





Week 12:

Assay1.jpg
MptpB enzyme assay with pNPP as surrogate substrate


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MptpB after FPLC and viva spin, trial 1


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trial 2


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MptpB (induced after OD600 = 0.8 for 5hrs at 30 degrees Centigrade) post FPLC purification, trial 1


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trial 2




Week 11:
  • Of the 30,000 ligands in the MW set, I have tested ligands 2,001-18,000. None of these ligands yielded higher fitness scores than the ligands we chose to order. The top two ligand scores obtained from the first 2,000 ligands (sceened last week) were 98.66 and 88.14. The top five scores obtained this week (ligands 2,001-18,000) are listed below.

JPB_Top5_MW_2001_18000_111311.jpg


Week 10:

OpenHouse.jpg


Week 9:
  • Grew up 1.5L of LB + BL21 and most likely ruined the protein
  • Grew up 3L of LB + BL21 inducing after 0.8 OD600. This value was reached 1hr 40min after addition of overnight growth. Next time, will use less overnight growth in 1L LB samples in order to catch an OD600 of 0.3.



Week 8:
  • FPLC purified MptpB
  • Concentrated and obtained the following readings

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Concentrated MptpB after FPLC (1st reading)


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2nd reading


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3rd reading

  • First inhibition assay

MptpBAssay1.jpg



Week 7:
  • Out



Week 6:
  • Lysed two bacterial pellets
  • Purified 2 samples independently (approx. 15 mL each)
  • Ran a gel using the sample that had a concentration 0.19 mg/mL

JPBGelPic.jpg
Lane 1: Skipped, Lane 2: PageRuler Prestained Protein, Lane 3: Soluble Fraction, Lane 4: Flow through, Lane 5: Wash, Lane 6: Elution #1, Lane 7: Elution #2


  • Concentrated Elution #1 and Wash for FPLC purification. A significant amount of MptpB was lost in the wash step.

- Joshua - avoid putting links to files here. Show results in a table or in a screenshot instead. -- Dr. B



Week 5:
  • Worked on Virtual Screening



Week 4:
  • Worked on PyMol



Week 3:
  • Transformed BL21 cells using the good, midi prepped plasmid sample
  • Picked two colonies, one from each of two plates, and grew up two samples for 12 hr overnight
  • Began to grow up protein (two 550mL samples of BL21 cells + LB + Kan left on the counter for 1 hr)
  • Picked a colony from the plate that had 10 uL of transformed plasmid plated (colonies are bigger and more spread out as opposed to the plate that had 50 uL of plasmid plated) - trial 2 of the protein expression scale up
  • Pelleted two samples of BL21 bacteria (trial 1 samples had a wait period at room temp of 1 hr before IPTG was added and the trial 2 sample didn't have an exponential growth pattern)
  • Scaled up bacteria and grew up MptpB once again (trial three) using 1M K3PO4, 10% glycerol with LB + Kan for the overnight growth of one sample. For the second sample I re-suspended the bacteria in fresh LB + Kan after growing it up in LB + Kan (centrifuged BL21 cells at 6000g for 5 min). The 10% glycerol was used as an extra energy source and the K3PO4 was used as a buffer since the 50mL of LB from overnight growth becomes acidic. For one sample I simply re-suspended the bacteria in fresh LB.

GrowthCurveJPB.png
Sample A: 1M K3PO4, 10% glycerol used; Sample B: BL21 pelleted and re-suspended in fresh LB




Week 2:
  • Transformed DH5 alpha cells using the plasmid sample containing my GOI after it's been mini prepped

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Left plate: 50mL of transformed BL21 plated; Right plate: 10mL of transformed BL21 plated


  • Grew up transformed DH5 alpha cells and midi prepped them
  • Sent two samples to sequencing one of which had a 100% match with my GOI



Week 1:
  • Confirmed a 100% match for my GOI in pNIC-Bsa4

Good pNIC-Bsa4 + MptpB gene read after Midi Prep:

JPB1.jpg
Subject: reverse sequence; Query: forward sequence (The forward sequence has one N at 805 and the reverse sequence has an N at 716. The reverse sequence also has an insertion two nucloetides before the start codon since it has 859 instead of 858 bp.)

JPB2.jpg
Query: forward sequence + G replacing N determined from reverse sequence; Subject: GOI



Transformation Efficiency:


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1ng pGBR22: 3 colonies; transformation efficiency = 3000 (transformants/ug of plasmid)


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Figure 3: 5ng pGBR22: 560 colonies; transformation efficiency = 1.12e+5 (transformants/ug of plasmid)


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Figure 5: 25ng pGBR22: 23 colonies; transformation efficiency = 920 (transformants/ug of plasmid)


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Figure 7: Restriction Enzyme Digest and PCR: Lane 1: Skipped, Lane 2: 1kb DNA ladder, Lane 3: EcoRI digest, Lane 4: PvuII digest, Lane 5: EcoRI + PvuII digest, Lane 6: uncut plasmid, Lane 7: tube A PCR, Lane 8: tube B PCR, Lane 9: tube C PCR, Lane 10: tube D PCR


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Figure 8: First attempt at PCR for RE cloning


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Figure 9: RE cloning: Lane 1: Skipped, Lane 2: 100bp Ladder, Lane 3: 0.016ng pGFP amplified using VDS1 and 2, Lane 4: 0.16ng pGFP amplified using VDS1 and 2, Lane 5: 1.6ng pGFP amplified using VDS1 and 2, Lane 6: Skipped, Lane 7: No DNA, Lane 8: Skipped, Lane 9: 0.016ng pGFP amplified using M13For and Rev, Lane 10: 0.16ng pGFP amplified using M13For and Rev, Lane 11: 1.6ng pGFP amplified using M13For and Rev, Lane 12: No DNA




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Figure 12: First attempt at PCR for pLIC sequencing vectors of pNIC-Bsa4


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Figure 13: PCR for pLIC sequencing vectors of pNIC-Bsa4




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Figure 16: PCR for pLIC sequencing vectors of pNIC-Bsa4




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Figure 19: PCR for pNIC-Bsa4 cloning




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Figure 22: Option B of previous protocol(single best condition scaled up to 50ul)




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Figure 25: Lane 1: Skipped Lane 2: Ladder; Ruoyi Pu Lane 3: Primary PCR Lane 4: Secondary PCR; Jeanette C. Lane 5: Primary PCR Lane 6: Secondary PCR; Sadhana B. Lane 7: Primary PCR Lane 8: Secondary PCR; Josh B. Lane 9: Primary PCR Lane 10: Secondary PCR




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Figure 28: Lane 1: 100bp ladder, Lane 2: PCR^2 product


The top band matches up with the secondary PCR product. However, there appears to be another smaller band. The forward and reverse primers were probably used to amplify both strands. I continued with the cloning procedure despite the fact that my PCR^2 product appears to contain two amplified sequences.


PCR^2_after_cleanup.png
Figure 30: Lane 1:100bp ladder, Lane 2: Skipped, Lane 3: PCR^2 product after PCR cleanup


The lower band appears much brighter than the upper (desired) band after PCR cleanup. Some of the MPTPb coding sequence may have not been eluted properly.



The pNIC-Bsa4 fragments don't appear because I mistakenly used 2.25 ng when treating with BsaI rather than 2.25 ug, the amount called for in the protocol for pNIC-Bsa4 cloning.

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Figure 31: Lane 1: Skipped, Lane 2: 100bp ladder, Lane 3: primary PCR product, Lanes 4-8: Secondary PCR w/regular primers, Lane 9: pNIC-Bsa4 after treatment with BsaI


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Figure 34: PCR^2 for trial 2 of version 2 of cloning: Lane 1: 100bp ladder, Lane 2: Skipped, Lanes 3-6: PCR^2 product





SHOT2.png
Figure 37: Lane 1: Skipped, Lane 2: 100bp ladder, Lane 3: primary PCR product sample 1, Lanes 4-5: PCR^2 product (sample 1 of primary PCR product and designed primers used), Lane 6: primary PCR product sample 2, Lanes 7-8: (sample 2 of primary PCR product and designed primers used)